view article

Figure 2
Superposition of the Cα traces of the two core domains of representative GH30 enzymes. Sa16Gal30A (PDB entry 24td, GH30_5) is shown in black, human acid β-glucosidase (HsGCase; PDB entry 1y7v, GH30_1) in cyan, Bacteroides thetaiotaomicron VPI-5482 endo-β-1,6-glucanase BT3312 (PDB entry 5ngl, GH30_3) in blue, an uncharacterized Bacteroides fragilis protein BF1510 (PDB entry 3clw, subfamily GH30_4) in green, Talaromyces cellulolyticus endo-glucuronoxylanase Xyn30B (PDB entry 6krn, GH30_7) in pink, Dickeya chrysanthemi glucuronoxylanase XynA (PDB entry 2y24, GH30_8) in orange and Acetivibrio clariflavus xylobiohydrolase (AcXbh30; PDB entry 7n6o, GH30_10) in yellow. The Cα traces of the catalytic domains and the attached β-sandwich domains are shown. Signal peptides, tags and additional carbohydrate-binding modules are omitted. Secondary-structure elements forming the (β/α)8-barrel are indicated by red letters. The second, fourth and eighth loops of Sa16Gal30A are labeled.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Follow Acta Cryst. D
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds